BMRB Entry 53226

Name: 1H, 15N, and 13C resonance assignment of human heat shock protein 10 (Hsp10)
Published: 2025-11-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53226

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 15N, and 13C resonance assignment of human heat shock protein 10 (Hsp10)

Deposition date:

2025-06-13

Original release date:

2025-11-11

Authors:

Page, Abigail; Hendricks, Wyatt; Walti, Marielle

Citation:

Citation: Page, Abigail; Hendricks, Wyatt; Walti, Marielle. "1H, 15N, and 13C resonance assignment of human heat shock protein 10" Biomol. NMR Assign. 19, 287-292 (2025).
PubMed: 40944855

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAGQAFRKFLPLFDRVLVER SAAETVTKGGIMLPEKSQGK VLQATVVAVGSGSKGKGGEI QPVSVKVGDKVLLPEYGGTK VVLDDKDYFLFRDGDILGKY VD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	244
15N chemical shifts	92
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hsp10k, chain 1	1
2	Hsp10k, chain 2	1
3	Hsp10k, chain 3	1
4	Hsp10k, chain 4	1
5	Hsp10k, chain 5	1
6	Hsp10k, chain 6	1
7	Hsp10k, chain 7	1

Entities:

Entity 1, Hsp10k, chain 1 102 residues - Formula weight is not available

1

MET

ALA

GLY

GLN

ALA

PHE

ARG

LYS

PHE

LEU

2

PRO

LEU

PHE

ASP

ARG

VAL

LEU

VAL

GLU

ARG

3

SER

ALA

GLU

THR

VAL

THR

LYS

GLY

4

ILE

MET

LEU

PRO

GLU

LYS

SER

GLN

GLY

LYS

5

VAL

LEU

GLN

ALA

THR

VAL

ALA

VAL

GLY

6

SER

GLY

SER

LYS

GLY

LYS

GLY

GLU

ILE

7

GLN

PRO

VAL

SER

VAL

LYS

VAL

GLY

ASP

LYS

8

VAL

LEU

PRO

GLU

TYR

GLY

THR

LYS

9

VAL

LEU

ASP

LYS

ASP

TYR

PHE

LEU

10

PHE

ARG

ASP

GLY

ASP

ILE

LEU

GLY

LYS

TYR

11

VAL

ASP

Samples:

sample_1: Hsp10, [U-100% 13C; U-100% 15N], 900 uM; D2O 5%; sodium phosphate 40 mM; sodium azide .03%

sample_conditions_1: ionic strength: 0.071 M; pH: 7; pressure: 1 atm; temperature: 298-303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker AVANCE NEO 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks